Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C

FEBS Letters

Heinisch, Jürgen J¹  Schmitz, Hans-Peter¹  Jacoby, Jörg J¹ 

[1] Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, Geb. 26.12, D-40225 Düsseldorf, Germany

关键词: Protein kinase C;    Signal transduction;    In vitro mutagenesis;    Saccharomyces cerevisiae;   

DOI  :  10.1016/S0014-5793(97)01287-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In an attempt to study the functional similarities between protein kinase C from the yeast Saccharomyces cerevisiae and its human homologues we have started in vitro mutagenesis to alter specific domains. Here we report on the exchange of four cysteine residues by serines in yeast Pkc1p that have been shown to be essential for diacylglycerol (DAG) binding and activation by this compound in humans. The mutant yeast protein leads to sensitivity to caffeine and low concentrations of SDS when expressed in a pkc1 deletion strain. However, sensitivity to staurosporine was not affected. Our data indicate that the conserved DAG binding domain serves an important function in yeast Pkc1p.

【 授权许可】

Unknown